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The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution.

The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Research Abstract Details 

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  • The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Abstract Text:

    christina m sorensenChristina M Sorensen,lea a rempelLea A Rempel,shane r nelsonShane R Nelson,brian r francisBrian R Francis,david j perryDavid J Perry,randolph v lewisRandolph V Lewis,arthur l haasArthur L Haas,thomas r hansenThomas R Hansen,

    Interferon-stimulated gene (ISG) 15 mediates antiviral responses and also is upregulated within the endometrium in response to the developing embryo during early pregnancy. Structurally, ISG15 resembles two ubiquitin domains (30% identical) that are separated by a hinge region. Recombinant (r) bovISG15 is not stable in solution. It was hypothesized that the hinge region contributed to the instability of rbovISG15. Within 24 h of dialysis, rbovISG15 formed complexes as detected by reducing and denaturing SDS-PAGE. However, chemical perturbations of cysteine prevented formation of rbovISG15 complexes over time. Furthermore, a site-directed mutant of rbovISG15 (Cys80Ser) was isomeric and more stable than rbovISG15. Neither wild-type nor mutant rbovISG15 was able to interact with the ISG15 E1 initiating enzyme, UBE1L, in an in vitro pull-down assay. Ovine (ov) ISG15 has three additional amino acids within the hinge region that were hypothesized to increase stability and the degree of interaction with UBE1L because of increased separation of the ubiquitin-like domains. Over time in solution, rovISG15 the level of rovISG15 secondary structure was diminished, whereas the Cys80Ser rovISG15 structure did not change. A GST-Cys80Ser rovISG15 fusion protein had increased structural stability and enhanced protein-protein interaction with UBE1L after dialysis for 48 h, when compared to the GST-rovISG15 fusion protein or rbovISG15. Models of bovISG15, Cys80Ser bovISG15, and ovISG15 were constructed, which confirmed that the hinge region between the two ubiquitin domains destabilizes rbovISG15 in solution.

    The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Publishing Authors By Initials

    cm sorensenCM Sorensen,la rempelLA Rempel,sr nelsonSR Nelson,br francisBR Francis,dj perryDJ Perry,rv lewisRV Lewis,al haasAL Haas,tr hansenTR Hansen,

    For similar proteins: ubiquitins research abstracts see: proteins: ubiquitins research

    PUBMED ID PMID:

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    The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Biochemistry

    VOLUME: 46

    Page Numbers: 772-80

    Journal Abbreviation: Biochemistry

    ISSN: 0006-2960

    DAY: 23

    MONTH: Jan

    YEAR: 2007

    The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 370623

    The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Keywords Mesh Terms:

    KEYWORDS: Ubiquitins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution. Information

    Substance Name: Ubiquitin-Activating Enzymes

    Registry Number: EC 6.3.2.19

    Grant and Affiliation Information for The hinge region between two ubiquitin-like domains destabilizes recombinant ISG15 in solution.

    AFFILIATION: Department of Animal Science, University of Wyoming, Laramie, Wyoming 82071, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NCRR

    GRANT: P20 RR 015553

    ACRONYM: RR

    MEDLINETA: Biochemistry

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